S15.12 Inhibition of mammalian cytochrome bc1 complex by chromanols and related compounds
نویسندگان
چکیده
منابع مشابه
Crystallization of cytochrome bc1 complex.
Complex III (cytochrome bc1 particle; ubiquinol:ferricytochrome c oxidoreductase, EC 1.10.2.2) was purified from beef heart mitochondria by a combination of hydrophobic interaction and affinity chromatography. By washing the complex with detergent on the hydrophobic interaction column, phospholipids were effectively depleted; 7 mol of cardiolipin per mol of cytochrome c1 was retained in the fin...
متن کاملSuperoxide anion generation by the cytochrome bc1 complex.
We have measured the rates of superoxide anion generation by cytochrome bc(1) complexes isolated from bovine heart and yeast mitochondria and by cytochrome bc(1) complexes from yeast mutants in which the midpoint potentials of the cytochrome b hemes and the Rieske iron-sulfur cluster were altered by mutations in those proteins. With all of the bc(1) complexes the rate of superoxide anion produc...
متن کاملInhibition of the yeast cytochrome bc1 complex by ilicicolin H, a novel inhibitor that acts at the Qn site of the bc1 complex.
Ilicicolin H is an antibiotic isolated from the "imperfect" fungus Cylindrocladium iliciola strain MFC-870. Ilicicolin inhibits mitochondrial respiration by inhibiting the cytochrome bc(1) complex. In order to identify the site of ilicicolin action within the bc(1) complex we have characterized the effects of ilicicolin on the cytochrome bc(1) complex of Saccharomyces cerevisiae. Ilicicolin inh...
متن کاملProtonmotive pathways and mechanisms in the cytochrome bc1 complex.
The cytochrome bc(1) complex catalyzes electron transfer from ubiquinol to cytochrome c by a protonmotive Q cycle mechanism in which electron transfer is linked to proton translocation across the inner mitochondrial membrane. In the Q cycle mechanism proton translocation is the net result of topographically segregated reduction of quinone and reoxidation of quinol on opposite sides of the membr...
متن کاملThe rate-limiting step in the cytochrome bc1 complex (Ubiquinol-Cytochrome c Oxidoreductase) is not changed by inhibition of cytochrome b-dependent deprotonation: implications for the mechanism of ubiquinol oxidation at center P of the bc1 complex.
Quinol oxidation at center P of the cytochrome bc(1) complex involves bifurcated electron transfer to the Rieske iron-sulfur protein and cytochrome b. It is unknown whether both electrons are transferred from the same domain close to the Rieske protein, or if an unstable semiquinone anion intermediate diffuses rapidly to the vicinity of the b(L) heme. We have determined the pre-steady state rat...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 2008
ISSN: 0005-2728
DOI: 10.1016/j.bbabio.2008.05.410